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Protein

Tryptophan biosynthesis protein TrpCF

Gene

trpC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Bifunctional enzyme that catalyzes two sequential steps of tryptophan biosynthetic pathway. The first reaction is catalyzed by the isomerase, coded by the TrpF domain; the second reaction is catalyzed by the synthase, coded by the TrpC domain.

Catalytic activityi

N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate.
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO2 + H2O.

Pathwayi

GO - Molecular functioni

  1. indole-3-glycerol-phosphate synthase activity Source: EcoCyc
  2. phosphoribosylanthranilate isomerase activity Source: EcoCyc

GO - Biological processi

  1. tryptophan biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Isomerase, Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Tryptophan biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:PRAI-IGPS.
ECOL316407:JW1254-MONOMER.
MetaCyc:PRAI-IGPS.
BRENDAi5.3.1.24. 2026.
UniPathwayiUPA00035; UER00042.
UPA00035; UER00043.

Names & Taxonomyi

Protein namesi
Recommended name:
Tryptophan biosynthesis protein TrpCF
Including the following 2 domains:
Indole-3-glycerol phosphate synthase (EC:4.1.1.48)
Short name:
IGPS
N-(5'-phospho-ribosyl)anthranilate isomerase (EC:5.3.1.24)
Short name:
PRAI
Gene namesi
Name:trpC
Synonyms:trpF
Ordered Locus Names:b1262, JW1254
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11026. trpC.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 453453Tryptophan biosynthesis protein TrpCFPRO_0000154277Add
BLAST

Proteomic databases

PaxDbiP00909.
PRIDEiP00909.

Expressioni

Gene expression databases

GenevestigatoriP00909.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

IntActiP00909. 7 interactions.
STRINGi511145.b1262.

Structurei

Secondary structure

1
453
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 2319Combined sources
Helixi26 – 283Combined sources
Helixi30 – 323Combined sources
Helixi40 – 445Combined sources
Beta strandi46 – 483Combined sources
Beta strandi50 – 556Combined sources
Beta strandi57 – 593Combined sources
Turni60 – 623Combined sources
Beta strandi63 – 653Combined sources
Helixi71 – 788Combined sources
Turni79 – 813Combined sources
Beta strandi83 – 886Combined sources
Turni92 – 943Combined sources
Helixi100 – 1078Combined sources
Beta strandi112 – 1165Combined sources
Helixi121 – 1299Combined sources
Beta strandi133 – 1386Combined sources
Turni139 – 1413Combined sources
Helixi144 – 15613Combined sources
Beta strandi160 – 1656Combined sources
Helixi168 – 1769Combined sources
Beta strandi180 – 1878Combined sources
Turni189 – 1913Combined sources
Helixi197 – 20610Combined sources
Beta strandi210 – 2167Combined sources
Helixi221 – 2277Combined sources
Turni228 – 2303Combined sources
Beta strandi232 – 2365Combined sources
Helixi238 – 2414Combined sources
Helixi246 – 25510Combined sources
Helixi266 – 27510Combined sources
Beta strandi278 – 2836Combined sources
Helixi294 – 30310Combined sources
Beta strandi307 – 3148Combined sources
Helixi317 – 32711Combined sources
Beta strandi330 – 3345Combined sources
Helixi336 – 3383Combined sources
Helixi340 – 34910Combined sources
Beta strandi354 – 3618Combined sources
Beta strandi363 – 3653Combined sources
Beta strandi376 – 3816Combined sources
Helixi392 – 3954Combined sources
Beta strandi403 – 4086Combined sources
Turni411 – 4133Combined sources
Helixi414 – 4185Combined sources
Beta strandi423 – 4275Combined sources
Helixi429 – 4313Combined sources
Beta strandi432 – 4343Combined sources
Helixi440 – 45112Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JCMX-ray2.10P2-260[»]
1PIIX-ray2.00A2-453[»]
2KZHNMR-A256-385[»]
SMRiP00909. Positions 2-453.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00909.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 257257Indole-3-glycerol phosphate synthaseAdd
BLAST
Regioni258 – 453196N-(5'-phosphoribosyl)anthranilate isomeraseAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the TrpC family.Curated
In the C-terminal section; belongs to the TrpF family.Curated

Phylogenomic databases

eggNOGiCOG0134.
HOGENOMiHOG000280458.
InParanoidiP00909.
KOiK13498.
OrthoDBiEOG6WT8JX.

Family and domain databases

Gene3Di3.20.20.70. 2 hits.
HAMAPiMF_00134_B. IGPS_B.
MF_00135. PRAI.
InterProiIPR013785. Aldolase_TIM.
IPR013798. Indole-3-glycerol_P_synth.
IPR001468. Indole-3-GlycerolPSynthase_CS.
IPR001240. PRAI.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamiPF00218. IGPS. 1 hit.
PF00697. PRAI. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 2 hits.
PROSITEiPS00614. IGPS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00909-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMQTVLAKIV ADKAIWVEAR KQQQPLASFQ NEVQPSTRHF YDALQGARTA
60 70 80 90 100
FILECKKASP SKGVIRDDFD PARIAAIYKH YASAISVLTD EKYFQGSFNF
110 120 130 140 150
LPIVSQIAPQ PILCKDFIID PYQIYLARYY QADACLLMLS VLDDDQYRQL
160 170 180 190 200
AAVAHSLEMG VLTEVSNEEE QERAIALGAK VVGINNRDLR DLSIDLNRTR
210 220 230 240 250
ELAPKLGHNV TVISESGINT YAQVRELSHF ANGFLIGSAL MAHDDLHAAV
260 270 280 290 300
RRVLLGENKV CGLTRGQDAK AAYDAGAIYG GLIFVATSPR CVNVEQAQEV
310 320 330 340 350
MAAAPLQYVG VFRNHDIADV VDKAKVLSLA AVQLHGNEEQ LYIDTLREAL
360 370 380 390 400
PAHVAIWKAL SVGETLPARE FQHVDKYVLD NGQGGSGQRF DWSLLNGQSL
410 420 430 440 450
GNVLLAGGLG ADNCVEAAQT GCAGLDFNSA VESQPGIKDA RLLASVFQTL

RAY
Length:453
Mass (Da):49,492
Last modified:March 19, 2014 - v4
Checksum:i09D5DA2353291F33
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 311Missing in CAA23673 (PubMed:7038627).Curated
Sequence conflicti95 – 951Q → R in CAA23664 (PubMed:7007653).Curated
Sequence conflicti95 – 951Q → R in AAA57299 (PubMed:7007653).Curated
Sequence conflicti95 – 951Q → R in CAA23673 (PubMed:7038627).Curated
Sequence conflicti285 – 2851Missing in CAA23673 (PubMed:7038627).Curated
Sequence conflicti294 – 2941V → D in CAA23673 (PubMed:7038627).Curated
Sequence conflicti330 – 3301A → V in CAA23664 (PubMed:7007653).Curated
Sequence conflicti330 – 3301A → V in AAA57299 (PubMed:7007653).Curated
Sequence conflicti330 – 3301A → V in CAA23673 (PubMed:7038627).Curated
Sequence conflicti399 – 3991S → T in CAA23664 (PubMed:7007653).Curated
Sequence conflicti399 – 3991S → T in AAA57299 (PubMed:7007653).Curated
Sequence conflicti399 – 3991S → T in CAA23673 (PubMed:7038627).Curated
Sequence conflicti399 – 3991S → T in AAB60033 (PubMed:8095913).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00366 Genomic DNA. Translation: CAA23664.1.
V00372 Genomic DNA. Translation: CAA23673.1.
J01714 Genomic DNA. Translation: AAA57299.1.
U23489 Genomic DNA. Translation: AAB60033.1.
U00096 Genomic DNA. Translation: AAC74344.3.
AP009048 Genomic DNA. Translation: BAA14794.1.
PIRiA64874. GWEC.
RefSeqiNP_415778.3. NC_000913.3.
YP_489530.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74344; AAC74344; b1262.
BAA14794; BAA14794; BAA14794.
GeneIDi12931128.
945519.
KEGGiecj:Y75_p1236.
eco:b1262.
PATRICi32117784. VBIEscCol129921_1312.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00366 Genomic DNA. Translation: CAA23664.1.
V00372 Genomic DNA. Translation: CAA23673.1.
J01714 Genomic DNA. Translation: AAA57299.1.
U23489 Genomic DNA. Translation: AAB60033.1.
U00096 Genomic DNA. Translation: AAC74344.3.
AP009048 Genomic DNA. Translation: BAA14794.1.
PIRiA64874. GWEC.
RefSeqiNP_415778.3. NC_000913.3.
YP_489530.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JCMX-ray2.10P2-260[»]
1PIIX-ray2.00A2-453[»]
2KZHNMR-A256-385[»]
SMRiP00909. Positions 2-453.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP00909. 7 interactions.
STRINGi511145.b1262.

Proteomic databases

PaxDbiP00909.
PRIDEiP00909.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74344; AAC74344; b1262.
BAA14794; BAA14794; BAA14794.
GeneIDi12931128.
945519.
KEGGiecj:Y75_p1236.
eco:b1262.
PATRICi32117784. VBIEscCol129921_1312.

Organism-specific databases

EchoBASEiEB1019.
EcoGeneiEG11026. trpC.

Phylogenomic databases

eggNOGiCOG0134.
HOGENOMiHOG000280458.
InParanoidiP00909.
KOiK13498.
OrthoDBiEOG6WT8JX.

Enzyme and pathway databases

UniPathwayiUPA00035; UER00042.
UPA00035; UER00043.
BioCyciEcoCyc:PRAI-IGPS.
ECOL316407:JW1254-MONOMER.
MetaCyc:PRAI-IGPS.
BRENDAi5.3.1.24. 2026.

Miscellaneous databases

EvolutionaryTraceiP00909.
PROiP00909.

Gene expression databases

GenevestigatoriP00909.

Family and domain databases

Gene3Di3.20.20.70. 2 hits.
HAMAPiMF_00134_B. IGPS_B.
MF_00135. PRAI.
InterProiIPR013785. Aldolase_TIM.
IPR013798. Indole-3-glycerol_P_synth.
IPR001468. Indole-3-GlycerolPSynthase_CS.
IPR001240. PRAI.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamiPF00218. IGPS. 1 hit.
PF00697. PRAI. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 2 hits.
PROSITEiPS00614. IGPS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Gene structure in the tryptophan operon of Escherichia coli. Nucleotide sequence of trpC and the flanking intercistronic regions."
    Christie G.E., Platt T.
    J. Mol. Biol. 142:519-530(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Nucleotide sequence of the trpD and trpC genes of Salmonella typhimurium."
    Horowitz H., van Arsdell J., Platt T.
    J. Mol. Biol. 169:775-797(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 95 AND 399.
  3. "The complete nucleotide sequence of the tryptophan operon of Escherichia coli."
    Yanofsky C., Platt T., Crawford I.P., Nichols B.P., Christie G.E., Horowitz H., van Cleemput M., Wu A.M.
    Nucleic Acids Res. 9:6647-6668(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Molecular evolution of the Escherichia coli chromosome. IV. Sequence comparisons."
    Milkman R., Bridges M.M.
    Genetics 133:455-468(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  7. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  8. "Deep coverage of the Escherichia coli proteome enables the assessment of false discovery rates in simple proteogenomic experiments."
    Krug K., Carpy A., Behrends G., Matic K., Soares N.C., Macek B.
    Mol. Cell. Proteomics 12:3420-3430(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-8.
    Strain: K12 / BW25113.
  9. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  10. "Three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate isomerase: indoleglycerolphosphate synthase from Escherichia coli refined at 2.0-A resolution."
    Wilmanns M., Priestle J.P., Niermann T., Jansonius J.N.
    J. Mol. Biol. 223:477-507(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SEQUENCE REVISION TO 320.
  11. "Crystallization and structure solution at 4-A resolution of the recombinant synthase domain of N-(5'-phosphoribosyl)anthranilate isomerase:indole-3-glycerol-phosphate synthase from Escherichia coli complexed to a substrate analogue."
    Wilmanns M., Schlagenhauf E., Fol B., Jansonius J.N.
    Protein Eng. 3:173-180(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 258-453.

Entry informationi

Entry nameiTRPC_ECOLI
AccessioniPrimary (citable) accession number: P00909
Secondary accession number(s): P78059, P78234, P94704
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 19, 2014
Last modified: April 1, 2015
This is version 147 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.